Structural similarities and differences in H‐ NS family proteins revealed by the N‐terminal structure of TurB in Pseudomonas putida KT 2440

H‐ NS family proteins play key roles in bacterial nucleoid compaction and global transcription. MvaT homologues in Pseudomonas have almost negligible amino acid sequence identity with H‐ NS , but can complement an hns ‐related phenotype of Escherichia coli . Here, we report the crystal structure of the N‐terminal dimerization/oligomerization domain of TurB, an MvaT homologue in Pseudomonas putida KT 2440. Our data identify two dimerization sites; the structure of the central dimerization site is almost the same as the corresponding region of H‐ NS , whereas the terminal dimerization sites are different. Our results reveal similarities and differences in dimerization and oligomerization mechanisms between H‐ NS and TurB.